Peptide/protein tagging offers powerful ways to manipulate proteins in various contexts, such as protein purification, translocation, topology engineering, and bio-imaging.  The recent emergence of “molecular superglue” techniques provides a new tagging strategy with essentially infinite affinity, as demonstrated by the SpyTag/SpyCatcher, SnoopTag/SnoopCatcher reactive pairs as well as their variants. They are based entirely on natural amino acids and are thus genetically encodable. Incorporating latent bio-reactive unnatural amino acids represents another way to achieve covalent tagging or bioconjugation via proximity-enhanced reaction. It can be readily achieved both in vitro and in vivo in various cells, leaving only a tiny residue after ligation. By contrast, genetically en coded peptide-protein reactive pairs often forms a complex after ligation which may complicate the study of structure-property relationship. 

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